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A more recent version of this article appeared on November 1, 2003
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Submitted on June 10, 2003
Revised on July 18, 2003
Accepted on July 18, 2003
1 The Rockefeller University, New York, NY 10021
* Corresponding author. E-mail address: fcross{at}mail.rockefeller.edu.
We evaluated the hypothesis that the N-terminal region of the
replication control protein Cdc6 acts as an inhibitor of
cyclin-dependent kinase (Cdk) activity, promoting mitotic exit (Calzada
et al., 2001). Cdc6 accumulation is restricted to the
period from midcell cycle until the succeeding G1, due to proteolytic
control that requires the Cdc6 N-terminal region. During late mitosis,
Cdc6 is present at levels comparable to Sic1, and binds specifically to
the mitotic cyclin Clb2. Moderate overexpression of Cdc6 promotes
viability of CLB2
db strains, which otherwise arrest
at mitotic exit, and rescue is dependent on the N-terminal putative
Cdk-inhibitory domain. These observations support the potential for
Cdc6 to inhibit Clb2-Cdk, thus promoting mitotic exit. Consistent with
this idea, we observed a cytokinesis defect in cdh1
sic1 cdc62-49 triple mutants. However, we
were able to construct viable strains, in three different backgrounds,
containing neither SIC1 nor the Cdc6 Cdk-inhibitory
domain, in contradiction to Calzada et al. (2001). We
conclude, therefore, that while both Cdc6 and Sic1 have the potential
to facilitate mitotic exit by inhibiting Clb2-Cdk, mitotic exit
nevertheless does not require any identified stoichiometric inhibitor
of Cdk activity.
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